Caveolin-1-Mediated Apolipoprotein A-I Membrane Binding Sites Are Not Required for Cholesterol Efflux
Identifieur interne : 006581 ( Main/Merge ); précédent : 006580; suivant : 006582Caveolin-1-Mediated Apolipoprotein A-I Membrane Binding Sites Are Not Required for Cholesterol Efflux
Auteurs : Soazig Le Lay [France] ; Macarena Rodriguez [Australie] ; Wendy Jessup [Australie] ; Carles Rentero [Australie] ; Qiong Li [Australie] ; Siân Cartland [Australie] ; Thomas Grewal [Australie] ; Katharina Gaus [Australie]Source :
- PLoS ONE [ 1932-6203 ] ; 2011.
Abstract
Caveolin-1 (Cav1), a structural protein required for the formation of invaginated membrane domains known as caveolae, has been implicated in cholesterol trafficking and homeostasis. Here we investigated the contribution of Cav1 to apolipoprotein A-I (apoA-I) cell surface binding and intracellular processing using mouse embryonic fibroblasts (MEFs) derived from wild type (WT) or Cav1-deficient (Cav1−/−) animals. We found that cells expressing Cav1 have 2.6-fold more apoA-I binding sites than Cav1−/− cells although these additional binding sites are not associated with detergent-free lipid rafts. Further, Cav1-mediated binding targets apoA-I for internalization and degradation and these processes are not correlated to cholesterol efflux. Despite lower apoA-I binding, cholesterol efflux from Cav1−/− MEFs is 1.7-fold higher than from WT MEFs. Stimulation of ABCA1 expression with an LXR agonist enhances cholesterol efflux from both WT and Cav1−/− cells without increasing apoA-I surface binding or affecting apoA-I processing. Our results indicate that there are at least two independent lipid binding sites for apoA-I; Cav1-mediated apoA-I surface binding and uptake is not linked to cholesterol efflux, indicating that membrane domains other than caveolae regulate ABCA1-mediated cholesterol efflux.
Url:
DOI: 10.1371/journal.pone.0023353
PubMed: 21858084
PubMed Central: 3155548
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Required for Cholesterol Efflux</title><author><name sortKey="Le Lay, Soazig" sort="Le Lay, Soazig" uniqKey="Le Lay S" first="Soazig" last="Le Lay">Soazig Le Lay</name><affiliation wicri:level="3"><nlm:aff id="aff1"><addr-line>Centre de Recherche des Cordeliers, INSERM, U872, Paris, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Centre de Recherche des Cordeliers, INSERM, U872, Paris</wicri:regionArea><placeName><region type="region">Île-de-France</region><region type="old region">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Rodriguez, Macarena" sort="Rodriguez, Macarena" uniqKey="Rodriguez M" first="Macarena" last="Rodriguez">Macarena Rodriguez</name><affiliation wicri:level="3"><nlm:aff id="aff2"><addr-line>Centre for Vascular Research, University of New South Wales, Sydney, Australia</addr-line></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Centre 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type="état">Nouvelle-Galles du Sud</region><settlement type="city">Sydney</settlement></placeName><orgName type="university">Université de Sydney</orgName></affiliation></author><author><name sortKey="Gaus, Katharina" sort="Gaus, Katharina" uniqKey="Gaus K" first="Katharina" last="Gaus">Katharina Gaus</name><affiliation wicri:level="3"><nlm:aff id="aff2"><addr-line>Centre for Vascular Research, University of New South Wales, Sydney, Australia</addr-line></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Centre for Vascular Research, University of New South Wales, Sydney</wicri:regionArea><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region></placeName></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Caveolin-1 (Cav1), a structural protein required for the formation of invaginated membrane domains known as caveolae, has been implicated in cholesterol trafficking and homeostasis. Here we investigated the contribution of Cav1 to apolipoprotein A-I (apoA-I) cell surface binding and intracellular processing using mouse embryonic fibroblasts (MEFs) derived from wild type (WT) or Cav1-deficient (Cav1<sup>−/−</sup>) animals. We found that cells expressing Cav1 have 2.6-fold more apoA-I binding sites than Cav1<sup>−/−</sup> cells although these additional binding sites are not associated with detergent-free lipid rafts. Further, Cav1-mediated binding targets apoA-I for internalization and degradation and these processes are not correlated to cholesterol efflux. Despite lower apoA-I binding, cholesterol efflux from Cav1<sup>−/−</sup> MEFs is 1.7-fold higher than from WT MEFs. Stimulation of ABCA1 expression with an LXR agonist enhances cholesterol efflux from both WT and Cav1<sup>−/−</sup> cells without increasing apoA-I surface binding or affecting apoA-I processing. Our results indicate that there are at least two independent lipid binding sites for apoA-I; Cav1-mediated apoA-I surface binding and uptake is not linked to cholesterol efflux, indicating that membrane domains other than caveolae regulate ABCA1-mediated cholesterol efflux.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Parton, Rg" uniqKey="Parton R">RG Parton</name></author><author><name sortKey="Simons, K" uniqKey="Simons K">K Simons</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Razani, B" uniqKey="Razani B">B Razani</name></author><author><name sortKey="Engelman, Ja" uniqKey="Engelman J">JA Engelman</name></author><author><name sortKey="Wang, Xb" uniqKey="Wang X">XB Wang</name></author><author><name sortKey="Schubert, W" uniqKey="Schubert W">W Schubert</name></author><author><name sortKey="Zhang, Xl" uniqKey="Zhang X">XL 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